scholarly journals Synthetic RNAs Mimicking Structural Domains in the Foot-and-Mouth Disease Virus Genome Elicit a Broad Innate Immune Response in Porcine Cells Triggered by RIG-I and TLR Activation

Viruses ◽  
2015 ◽  
Vol 7 (7) ◽  
pp. 3954-3973 ◽  
Author(s):  
Belén Borrego ◽  
Miguel Rodríguez-Pulido ◽  
Concepción Revilla ◽  
Belén Álvarez ◽  
Francisco Sobrino ◽  
...  
Keyword(s):  
Immune Response ◽  
Disease Virus ◽  
Innate Immune Response ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Innate Immune ◽  
Structural Domains ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids

1999 ◽  
Vol 80 (8) ◽  
pp. 1911-1918 ◽  
Author(s):  
Fiona M. Ellard ◽  
Jeff Drew ◽  
Wendy E. Blakemore ◽  
David I. Stuart ◽  
Andrew M. Q. King
Keyword(s):  
Disease Virus ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Dipole Interaction ◽  
Virus Genome ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Acidic Conditions ◽  
Α Helix

Foot-and-mouth disease virus (FMDV) capsids are inherently labile under mildly acidic conditions, dissociating to pentamers at pH values in the region of 6·5, with the release of protein 1A and the viral RNA. This acid-induced disassembly is thought to be required for the entry of the virus genome into the host cell. Previous work has highlighted a histidine–α-helix charge-dipole interaction at the twofold axes of symmetry between pentamers and has suggested that this interaction plays a role in acid-induced disassembly. The validity of this theory has now been tested by converting the implicated residue, His-142 of protein 1C, to Arg, Phe and Asp. The effects of such changes were studied by using a previously described vaccinia virus expression system, in which synthesis and processing of FMDV capsid proteins results in the self-assembly of capsids. In agreement with the histidine–α-helix charge-dipole theory, assembly in the arginine mutant was found to be greatly reduced, while capsids of the aspartic acid mutant were considerably more stable under acidic conditions than the wild-type. Aberrant but acid-stable complexes were obtained in the phenylalanine mutant.

scholarly journals Mutagenesis Mapping of RNA Structures within the Foot-and-Mouth Disease Virus Genome Reveals Functional Elements Localized in the Polymerase (3D pol )-Encoding Region

mSphere ◽  
2021 ◽  
Author(s):  
Lidia Lasecka-Dykes ◽  
Fiona Tulloch ◽  
Peter Simmonds ◽  
Garry A. Luke ◽  
Paolo Ribeca ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Rna Structures ◽  
Nonstructural Proteins ◽  
Functional Elements ◽  
Subgenomic Replicon ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Some RNA structures formed by the genomes of RNA viruses are critical for viral replication. Our study shows that of 46 conserved RNA structures located within the regions of the foot-and-mouth disease virus (FMDV) genome that encode the nonstructural proteins, only 3 are essential for replication of an FMDV subgenomic replicon.

scholarly journals Biochemical Mapping of the Foot-and-Mouth Disease Virus Genome

1977 ◽  
Vol 35 (2) ◽  
pp. 281-297 ◽  
Author(s):  
D. V. Sangar ◽  
D. N. Black ◽  
D. J. Rowlands ◽  
F. Brown
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals The broad-spectrum antiviral drug arbidol inhibits foot-and-mouth disease virus genome replication

2019 ◽  
Vol 100 (9) ◽  
pp. 1293-1302 ◽  
Author(s):  
Morgan R. Herod ◽  
Oluwapelumi O. Adeyemi ◽  
Joseph Ward ◽  
Kirsten Bentley ◽  
Mark Harris ◽  
...  
Keyword(s):  
Disease Virus ◽  
Broad Spectrum ◽  
Antiviral Drug ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Genome Replication ◽  
Mouth Disease Virus ◽  
Foot And Mouth
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